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Published on: May 3, 2018
Control of histone H3 phosphorylation by CaMKIIδ in response to haemodynamic cardiac stress
Salma Awad1, Kamar Mohamed Adib Al-Haffar, Qussay Marashly
1Cardiovascular Research Programme, King Faisal Specialist Hospital and Research Centre, Riyadh, Kingdom of Saudi Arabia.
Insights
Calcium/calmodulin-dependent protein kinase II delta (CaMKIIδ) regulates histone H3 phosphorylation, a key epigenetic mechanism driving fetal gene reactivation in cardiac hypertrophy and heart failure.
Area of Science:
- Molecular Biology
- Epigenetics
- Cardiovascular Research
Background:
- Heart failure involves reactivation of fetal cardiac genes, linked to cardiac hypertrophy and ventricular remodeling.
- Mechanisms regulating this transcriptional reprogramming in heart failure remain unclear.
Purpose of the Study:
- To investigate the role of calcium/calmodulin-dependent protein kinase II delta (CaMKIIδ) in regulating transcriptional reprogramming during cardiac hypertrophy.
- To elucidate the epigenetic mechanisms involving histone H3 phosphorylation in pathological cardiac remodeling.
Main Methods:
- Utilized genetically modified mice lacking CaMKIIδ (CaMKIIδ-deficient) subjected to pressure overload.
- Analyzed histone H3 serine-10 phosphorylation (H3 S10ph) levels in mouse hearts and human failing hearts.
- Investigated the interaction of CaMKIIδ with phospho-H3 and the role of 14-3-3 protein in transcriptional elongation.
Main Results:
- CaMKIIδ deficiency conferred resistance to pathological cardiac stress and abolished H3 S10ph.
- Increased H3 S10ph correlated with CaMKIIδ upregulation and fetal gene expression in hypertrophic hearts and human heart failure.
- CaMKIIδ recruitment and H3 S10ph at promoter regions activated fetal genes; 14-3-3 binding to phospho-H3 facilitated RNAPII elongation.
Conclusions:
- CaMKIIδ plays a critical role in regulating H3 S10 phosphorylation in response to cardiac stress.
- This CaMKIIδ-mediated epigenetic modification is a novel mechanism controlling fetal gene expression in cardiac hypertrophy.
- Findings suggest CaMKIIδ as a potential therapeutic target for heart failure by modulating epigenetic reprogramming.
Abstract:
Heart failure is associated with the reactivation of a fetal cardiac gene programme that has become a hallmark of cardiac hypertrophy and maladaptive ventricular remodelling, yet the mechanisms that regulate this transcriptional reprogramming are not fully understood. Using mice with genetic ablation of calcium/calmodulin-dependent protein kinase II δ (CaMKIIδ), which are resistant to pathological cardiac stress, we show that CaMKIIδ regulates the phosphorylation of histone H3 at serine-10 during pressure overload hypertrophy. H3 S10 phosphorylation is strongly increased in the adult mouse heart in the early phase of cardiac hypertrophy and remains detectable during cardiac decompensation. This response correlates with up-regulation of CaMKIIδ and increased expression of transcriptional drivers of pathological cardiac hypertrophy and of fetal cardiac genes. Similar changes are detected in patients with end-stage heart failure, where CaMKIIδ specifically interacts with phospho-H3. Robust H3 phosphorylation is detected in both adult ventricular myocytes and in non-cardiac cells in the stressed myocardium, and these signals are abolished in CaMKIIδ-deficient mice after pressure overload. Mechanistically, fetal cardiac genes are activated by increased recruitment of CaMKIIδ and enhanced H3 phosphorylation at hypertrophic promoter regions, both in mice and in human failing hearts, and this response is blunted in CaMKIIδ-deficient mice under stress. We also document that the chaperone protein 14-3-3 binds phosphorylated H3 in response to stress, allowing proper elongation of fetal cardiac genes by RNA polymerase II (RNAPII), as well as elongation of transcription factors regulating cardiac hypertrophy. These processes are impaired in CaMKIIδ-KO mice after pathological stress. The findings reveal a novel in vivo function of CaMKIIδ in regulating H3 phosphorylation and suggest a novel epigenetic mechanism by which CaMKIIδ controls cardiac hypertrophy.
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